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Helicobacter pylori and neutrophils: sialic acid-dependent binding to various isolated glycoconjugates.

Journal article
Authors Halina Miller-Podraza
Jörgen Bergström
Susann Teneberg
Maan Abul Milh
Marianne Longard
B M Olsson
L Uggla
Karl-Anders Karlsson
Published in Infection and immunity
Volume 67
Issue 12
Pages 6309-13
ISSN 0019-9567
Publication year 1999
Published at Institute of Medical Biochemistry
Pages 6309-13
Language en
Links www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Chromatography, Thin Layer, Electrophoresis, Polyacrylamide Gel, Gangliosides, metabolism, Glycoconjugates, chemistry, isolation & purification, metabolism, Glycoproteins, metabolism, Helicobacter pylori, growth & development, metabolism, Humans, N-Acetylneuraminic Acid, chemistry, Neutrophils, chemistry, metabolism
Subject categories Chemistry

Abstract

Helicobacter pylori has been shown to agglutinate erythrocytes in a sialic acid-dependent manner. However, very few studies have examined relevant target cells in the human stomach. Neutrophils are required for the onset of gastritis, and the inflammatory reaction may be induced on contact between bacteria and neutrophils. In the present work, glycolipids and glycoproteins were isolated from neutrophils and were studied for binding by overlay with radiolabeled bacteria on thin-layer chromatograms and on membrane blots. There was a complex pattern of binding bands. The only practical binding activity found was sialic acid dependent, since treatment of glycoconjugates with neuraminidase or mild periodate eliminated binding. As shown before for binding to erythrocytes and other glycoconjugates, bacterial cells grown on agar bound to many glycoconjugates, while growth in broth resulted in bacteria that would bind only to polyglycosylceramides, which are highly heterogeneous and branched poly-N-acetyllactosamine-containing glycolipids. Approximately seven positive bands were found for glycoproteins, and the traditional ganglioside fraction showed a complex, slow-moving interval with very strong sialic-acid-dependent binding, probably explained by Fuc substitutions on GlcNAc.

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